Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Sci. STKE, 2 July 2002
Vol. 2002, Issue 139, p. tw232
[DOI: 10.1126/stke.2002.139.tw232]


Neurobiology L1 Endocytosis

The neuronal cell adhesion molecule L1 regulates growth cone dynamics through extracellular interaction with other L1 molecules. Its cytoplasmic domain harbors a tyrosine-based sorting motif that interacts with the cell's clathrin machinery to facilitate its internalization. Schaefer et al. show that a single tyrosine residue within this motif is phosphorylated in vivo by the cytoplasmic tyrosine kinase Src. Phosphorylation prevented L1 binding to the adaptor protein AP-2 of the endocytosis machinery. L1-L1 interaction increased its dephosphorylation and increased its internalization into intracellular vesicles. The biochemical analysis suggests that cycles of phosphorylation and dephosphorylation regulate L1 availability in neurons.

A.W. Schaefer, Y. Kamei, H. Kamiguchi, E.V. Wong, I. Rapoport, T. Kirchhausen, C.M. Beach, G. Landreth, S.K. Lemmon, V. Lemmon, L1 endocytosis is controlled by a phosphorylation-dephosphorylation cycle stimulated by outside-in signaling by L1. J. Cell Biol. 157, 1223-1232 (2002). [Abstract] [Full Text]

Citation: L1 Endocytosis. Sci. STKE 2002, tw232 (2002).

To Advertise     Find Products

Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882